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P20618

- PSB1_HUMAN

UniProt

P20618 - PSB1_HUMAN

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Protein

Proteasome subunit beta type-1

Gene

PSMB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  5. apoptotic process Source: Reactome
  6. cellular nitrogen compound metabolic process Source: Reactome
  7. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  8. G1/S transition of mitotic cell cycle Source: Reactome
  9. gene expression Source: Reactome
  10. mitotic cell cycle Source: Reactome
  11. mRNA metabolic process Source: Reactome
  12. negative regulation of apoptotic process Source: Reactome
  13. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  14. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  15. protein polyubiquitination Source: Reactome
  16. regulation of apoptotic process Source: Reactome
  17. regulation of cellular amino acid metabolic process Source: Reactome
  18. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  19. RNA metabolic process Source: Reactome
  20. small molecule metabolic process Source: Reactome
  21. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_206597. Degradation of GLI2 by the proteasome.
REACT_228111. Hedgehog ligand biogenesis.
REACT_228209. Hh ligand biogenesis disease.
REACT_231645. GLI3 is processed to GLI3R by the proteasome.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_267605. Degradation of GLI1 by the proteasome.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Protein family/group databases

MEROPSiT01.986.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-1 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C5
Multicatalytic endopeptidase complex subunit C5
Proteasome component C5
Proteasome gamma chain
Gene namesi
Name:PSMB1
Synonyms:PSC5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:9537. PSMB1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProt
  5. proteasome complex Source: UniProtKB
  6. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33882.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 28281 PublicationPRO_0000259623Add
BLAST
Chaini29 – 241213Proteasome subunit beta type-1PRO_0000148030Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Glycosylationi58 – 581O-linked (GlcNAc)By similarity
Modified residuei150 – 1501PhosphotyrosineBy similarity
Modified residuei204 – 2041N6-acetyllysine1 Publication
Glycosylationi209 – 2091O-linked (GlcNAc)By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP20618.
PaxDbiP20618.
PeptideAtlasiP20618.
PRIDEiP20618.

2D gel databases

REPRODUCTION-2DPAGEIPI00025019.
UCD-2DPAGEP20618.

PTM databases

PhosphoSiteiP20618.

Expressioni

Gene expression databases

BgeeiP20618.
CleanExiHS_PSMB1.
GenevestigatoriP20618.

Organism-specific databases

HPAiCAB033911.
HPA029635.
HPA029637.

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with SERPINB2. Interacts with HIV-1 TAT protein.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMB5P280743EBI-372273,EBI-357828
PSMB7Q994368EBI-372273,EBI-603319

Protein-protein interaction databases

BioGridi111662. 102 interactions.
IntActiP20618. 21 interactions.
MINTiMINT-3009312.
STRINGi9606.ENSP00000262193.

Structurei

3D structure databases

ProteinModelPortaliP20618.
SMRiP20618. Positions 29-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000075035.
HOGENOMiHOG000091081.
HOVERGENiHBG000961.
InParanoidiP20618.
KOiK02732.
OMAiNAPEPEM.
OrthoDBiEOG7WHHBB.
PhylomeDBiP20618.
TreeFamiTF106218.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20618-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLSSTAMYSA PGRDLGMEPH RAAGPLQLRF SPYVFNGGTI LAIAGEDFAI
60 70 80 90 100
VASDTRLSEG FSIHTRDSPK CYKLTDKTVI GCSGFHGDCL TLTKIIEARL
110 120 130 140 150
KMYKHSNNKA MTTGAIAAML STILYSRRFF PYYVYNIIGG LDEEGKGAVY
160 170 180 190 200
SFDPVGSYQR DSFKAGGSAS AMLQPLLDNQ VGFKNMQNVE HVPLSLDRAM
210 220 230 240
RLVKDVFISA AERDVYTGDA LRICIVTKEG IREETVSLRK D
Length:241
Mass (Da):26,489
Last modified:May 1, 1992 - v2
Checksum:iAE8FC42799F39157
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111P → A.1 Publication
Corresponds to variant rs12717 [ dbSNP | Ensembl ].
VAR_051547
Natural varianti208 – 2081I → N.
Corresponds to variant rs10541 [ dbSNP | Ensembl ].
VAR_051548

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00761 mRNA. Translation: BAA00658.1.
BT019720 mRNA. Translation: AAV38525.1.
AB451312 mRNA. Translation: BAG70126.1.
AB451442 mRNA. Translation: BAG70256.1.
AL031259 Genomic DNA. Translation: CAA20287.1.
BC000508 mRNA. Translation: AAH00508.1.
BC020807 mRNA. Translation: AAH20807.1.
CCDSiCCDS34577.1.
PIRiS15973. SNHUC5.
RefSeqiNP_002784.1. NM_002793.3.
UniGeneiHs.352768.

Genome annotation databases

EnsembliENST00000262193; ENSP00000262193; ENSG00000008018.
GeneIDi5689.
KEGGihsa:5689.
UCSCiuc003qxr.3. human.

Polymorphism databases

DMDMi130853.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00761 mRNA. Translation: BAA00658.1 .
BT019720 mRNA. Translation: AAV38525.1 .
AB451312 mRNA. Translation: BAG70126.1 .
AB451442 mRNA. Translation: BAG70256.1 .
AL031259 Genomic DNA. Translation: CAA20287.1 .
BC000508 mRNA. Translation: AAH00508.1 .
BC020807 mRNA. Translation: AAH20807.1 .
CCDSi CCDS34577.1.
PIRi S15973. SNHUC5.
RefSeqi NP_002784.1. NM_002793.3.
UniGenei Hs.352768.

3D structure databases

ProteinModelPortali P20618.
SMRi P20618. Positions 29-241.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111662. 102 interactions.
IntActi P20618. 21 interactions.
MINTi MINT-3009312.
STRINGi 9606.ENSP00000262193.

Chemistry

BindingDBi P20618.
ChEMBLi CHEMBL4208.
DrugBanki DB00188. Bortezomib.
DB08889. Carfilzomib.

Protein family/group databases

MEROPSi T01.986.

PTM databases

PhosphoSitei P20618.

Polymorphism databases

DMDMi 130853.

2D gel databases

REPRODUCTION-2DPAGE IPI00025019.
UCD-2DPAGE P20618.

Proteomic databases

MaxQBi P20618.
PaxDbi P20618.
PeptideAtlasi P20618.
PRIDEi P20618.

Protocols and materials databases

DNASUi 5689.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262193 ; ENSP00000262193 ; ENSG00000008018 .
GeneIDi 5689.
KEGGi hsa:5689.
UCSCi uc003qxr.3. human.

Organism-specific databases

CTDi 5689.
GeneCardsi GC06M170844.
HGNCi HGNC:9537. PSMB1.
HPAi CAB033911.
HPA029635.
HPA029637.
MIMi 602017. gene.
neXtProti NX_P20618.
PharmGKBi PA33882.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000075035.
HOGENOMi HOG000091081.
HOVERGENi HBG000961.
InParanoidi P20618.
KOi K02732.
OMAi NAPEPEM.
OrthoDBi EOG7WHHBB.
PhylomeDBi P20618.
TreeFami TF106218.

Enzyme and pathway databases

Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_206597. Degradation of GLI2 by the proteasome.
REACT_228111. Hedgehog ligand biogenesis.
REACT_228209. Hh ligand biogenesis disease.
REACT_231645. GLI3 is processed to GLI3R by the proteasome.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_267605. Degradation of GLI1 by the proteasome.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

ChiTaRSi PSMB1. human.
GeneWikii PSMB1.
GenomeRNAii 5689.
NextBioi 22098.
PROi P20618.
SOURCEi Search...

Gene expression databases

Bgeei P20618.
CleanExi HS_PSMB1.
Genevestigatori P20618.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes)."
    Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H., Tanaka K., Ichihara A.
    Biochim. Biophys. Acta 1089:95-102(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-11.
    Tissue: Brain and Lung.
  6. "Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome)."
    Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N., Slaughter C.A.
    Biochim. Biophys. Acta 1037:178-185(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-52.
  7. "Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits."
    Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E.
    FEBS Lett. 553:200-204(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT.
  8. "Interaction of plasminogen activator inhibitor-2 and proteasome subunit, beta type 1."
    Fan J., Zhang Y.Q., Li P., Hou M., Tan L., Wang X., Zhu Y.S.
    Acta Biochim. Biophys. Sin. 36:42-46(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SERPINB2.
  9. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
    Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
    Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSB1_HUMAN
AccessioniPrimary (citable) accession number: P20618
Secondary accession number(s): B5BU76, Q9BWA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 1, 1992
Last modified: November 26, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3